Guo R F, Ward P A, Hu S M, McDuffie J E, Huber-Lang M, Shi M M
Genomic Pathology Laboratory, Department of Pathology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
Genomics. 1999 Jun 15;58(3):313-7. doi: 10.1006/geno.1999.5837.
By searching the Expressed Sequence Tag database, a full-length cDNA for a novel human CC chemokine was cloned. This cDNA encoded a 94-amino-acid protein with a putative signal peptide of 26 amino acids. The deduced mature protein had the four conserved cysteine residues characteristic of CC chemokines and showed 44% identity with MIP-1beta and 40% identity with MIP-1alpha, RANTES, and MCP-4. mRNA for this chemokine was expressed constitutively in human heart and liver and with lesser but detectable levels in skeletal muscle, kidney, and small intestine. To investigate its biological activity, the protein was expressed in mammalian cells and purified by affinity chromatography. The recombinant protein demonstrated chemotactic activity in vitro for T cells and monocytes but not for neutrophils. The gene was mapped to chromosome 7q11.2 by fluorescence in situ hybridization. Based on its structural identity with other CC chemokines and the chemotactic activity and chromosomal location of this chemokine, we designate this chemokine small inducible cytokine subfamily A, member 26 (SCYA26). This gene symbol has been approved by the HUGO Gene Nomenclature Committee.
通过搜索表达序列标签数据库，克隆到一种新型人类CC趋化因子的全长cDNA。该cDNA编码一种含有26个氨基酸的假定信号肽的94个氨基酸的蛋白质。推导的成熟蛋白具有CC趋化因子特有的四个保守半胱氨酸残基，与MIP-1β的同源性为44%，与MIP-1α、RANTES和MCP-4的同源性为40%。这种趋化因子的mRNA在人类心脏和肝脏中组成性表达，在骨骼肌、肾脏和小肠中的表达水平较低但可检测到。为了研究其生物学活性，该蛋白在哺乳动物细胞中表达并通过亲和层析纯化。重组蛋白在体外对T细胞和单核细胞表现出趋化活性，但对中性粒细胞没有趋化活性。通过荧光原位杂交将该基因定位于染色体7q11.2。基于其与其他CC趋化因子的结构同源性以及该趋化因子的趋化活性和染色体定位，我们将这种趋化因子命名为小诱导细胞因子亚家族A成员26（SCYA26）。这个基因符号已得到HUGO基因命名委员会的批准。
